AP1_CRYNH
ID AP1_CRYNH Reviewed; 700 AA.
AC J9VEC2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 2.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=AP-1-like transcription factor yap1 {ECO:0000303|PubMed:25445311};
DE AltName: Full=BZIP domain-containing transcription factor yap1 {ECO:0000303|PubMed:25445311};
GN Name=yap1 {ECO:0000303|PubMed:25445311}; ORFNames=CNAG_00239;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25445311; DOI=10.1016/j.fgb.2014.10.015;
RA Paul S., Doering T.L., Moye-Rowley W.S.;
RT "Cryptococcus neoformans Yap1 is required for normal fluconazole and
RT oxidative stress resistance.";
RL Fungal Genet. Biol. 74:1-9(2015).
CC -!- FUNCTION: Transcription activator involved in oxidative stress response
CC and redox homeostasis (PubMed:25445311). Regulates the transcription of
CC genes encoding antioxidant enzymes and components of the cellular
CC thiol-reducing pathways (By similarity). Involved in antifungal
CC resistance to fluconazole (PubMed:25445311).
CC {ECO:0000250|UniProtKB:Q4WMH0, ECO:0000269|PubMed:25445311}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q4WMH0}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q4WMH0}. Note=The nuclear localization is
CC oxidative stress-dependent and oxidized yap1 is found predominantly in
CC the nucleus, while reduced yap1 is continuously exported to the
CC cytoplasm. {ECO:0000250|UniProtKB:Q4WMH0}.
CC -!- DOMAIN: Contains two cysteine rich domains (CRD), referred to as the
CC N- and C-terminal CRD's, n-CRD and c-CRD, respectively. A nuclear
CC export signal is embedded in the c-CRD, with which the nuclear export
CC proteins interact only in the absence of disulfide bonds (or otherwise
CC oxidized cysteines) within the c-CRD or between the c-CRD and the n-
CC CRD. {ECO:0000250|UniProtKB:P19880}.
CC -!- PTM: Depending on the oxidative stress inducing agent, yap1 can undergo
CC two distinct conformational changes, both involving disulfide bond
CC formation, and both masking the nuclear export signal, thus abolishing
CC nuclear export. {ECO:0000250|UniProtKB:P19880}.
CC -!- DISRUPTION PHENOTYPE: Does not affect virulence.
CC {ECO:0000269|PubMed:25445311}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR EMBL; CP003820; AFR92373.2; -; Genomic_DNA.
DR RefSeq; XP_012046219.1; XM_012190829.1.
DR AlphaFoldDB; J9VEC2; -.
DR SMR; J9VEC2; -.
DR EnsemblFungi; AFR92373; AFR92373; CNAG_00239.
DR GeneID; 23884065; -.
DR VEuPathDB; FungiDB:CNAG_00239; -.
DR HOGENOM; CLU_395967_0_0_1; -.
DR Proteomes; UP000010091; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; DNA-binding; Nucleus; Oxidation; Transcription;
KW Transcription regulation.
FT CHAIN 1..700
FT /note="AP-1-like transcription factor yap1"
FT /id="PRO_0000449502"
FT DOMAIN 156..219
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 17..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..182
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 184..191
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 213..400
FT /note="Transcription activation 1"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 228..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..318
FT /note="n-CRD"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 320..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..577
FT /note="Transcription activation 2"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT REGION 542..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..675
FT /note="c-CRD"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT MOTIF 34..41
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 67..74
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 660..667
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:P19880"
FT COMPBIAS 44..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 666..675
FT /note="In nuclear retained form"
FT /evidence="ECO:0000250|UniProtKB:P19880"
SQ SEQUENCE 700 AA; 74750 MW; BC3AF6BF7B8C55A1 CRC64;
MQSALTPNTA AFLEYISPGH APTSAPPAAL FNNMPVPGRD TPEDTPPSVS NGSQPSAHQA
PSDDSDSPTP EMPPAQPDDA ANTDPLAGNG ANKRKAGRPS AVLDDDDDDA SDSDLPSGHE
DKKQHGAGRA AAASASGSGR RGRKSGGGEG DGKRELSKSE RRKEQNRAAQ KAFRERREAK
VKDLEDKVAE LENKAYGTQI ENENLRGILK RLQEENVALK QSAFTFSMPV NSRNSPNSNN
GSFSAPAPQN RKPLTPPQSS NDDSLKAVDD IPMLPHRHSS ANTISDNSSE SLVSLRSTDR
TPPALFSDHF NTYALGVVPV PPPSSSSQPT QKYPSASNGQ QSISSNSNSS NVISPPSADQ
SEFNALWESL YPNDVENLVS QNASQNQGGP FTLLNSQPDS MSFASAGNNN SMNALFNFGA
PSSPSISNSA QPSVNPAPAS VTQPANHITQ NLGATGQASD WNRFAFREPT AEASAPNWDL
TDNSVNEFLA SLSGDTTADA TANDYLNNDD EAFNAQLRKI FGNDNSPSAA FNLPSTSFSP
NNYLNMSPSP MMPLSNSQSP QSSDSRSNTN VSSGRGNDIS MADSPEYSMG SSRTSVSHDS
TDLQGKATTT TTTAIRSAKN YSCKSDNEVI HVVDEKGRVI KPSELWMRFG MQHENSTEHL
LIDDLCDQMR AKATCKDGKM QLDITDAAVL FRRGERRPSQ
